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Entry: A0A399G2E3_9ACTN
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ID   A0A399G2E3_9ACTN        Unreviewed;       394 AA.
AC   A0A399G2E3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   ORFNames=NI17_022805 {ECO:0000313|EMBL:UOE19510.1}, NI17_15095
GN   {ECO:0000313|EMBL:RII01856.1};
OS   Thermobifida halotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=483545 {ECO:0000313|EMBL:RII01856.1};
RN   [1] {ECO:0000313|EMBL:RII01856.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44931 {ECO:0000313|EMBL:RII01856.1};
RA   Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA   Herczeg R., Nagy I., Baka E., Kukolya J.;
RT   "De novo genome project of the cellulose decomposer Thermobifida
RT   halotolerans type strain.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:UOE19510.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE19510.1};
RA   Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT   "De novo genome project of the cellulose decomposer Thermobifida
RT   halotolerans type strain.";
RL   Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC         Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.12.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000126};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC         Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.12.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00001762};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SIMILARITY: Belongs to the globin family.
CC       {ECO:0000256|RuleBase:RU000356}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|ARBA:ARBA00006401}.
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DR   EMBL; JRUV01000265; RII01856.1; -; Genomic_DNA.
DR   EMBL; CP063196; UOE19510.1; -; Genomic_DNA.
DR   RefSeq; WP_068687452.1; NZ_LIZN01000001.1.
DR   AlphaFoldDB; A0A399G2E3; -.
DR   STRING; 483545.GCA_001660385_00063; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000265719; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd14782; FHb-globin_2; 1.
DR   CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43396; FLAVOHEMOPROTEIN; 1.
DR   PANTHER; PTHR43396:SF3; FLAVOHEMOPROTEIN; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00042; Globin; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000356}; Iron {ECO:0000256|RuleBase:RU000356};
KW   Metal-binding {ECO:0000256|RuleBase:RU000356};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265719};
KW   Transport {ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          5..129
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          153..262
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   394 AA;  42962 MW;  1D0B97C6C9FED773 CRC64;
     MLSPQSAEIV RATLPVVGAH LDQITARFYA TMFADRPELL DGLFNRANQA NGEQRRALAG
     SIAGFATALL DRPDERPDAM LARIAHKHAA VGVTEDQYVV VHKYLFGAIA DVLGEAVTPE
     VAAAWDEVYW LMGGALIAME ARIYAEKGAV NGRTWREWTI VDRREETPDV VSLTLRPDDD
     APLPEVRPGQ YVSVRMRMPD GVHQLRQYSV SGGDERSRRI TVKRVRGGRG APDGEMSTLL
     HADARVGDRL TVSAPFGDVV LTDGDRPLVL VSAGIGCTPI VGMLHHLAAT GATRRVLALH
     ADRSRDAHAL REETAELVDA LPRAERIVWY EEGDGGRTGR MDLGDVEIPA DAEVYLCGPV
     PFMRDARAQI LAAGVSARAV HYEVFGPDLW LPES
//
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